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Issue 64, 2018
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Binding and backbone dynamics of protein under topological constraint: calmodulin as a model system

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Abstract

Herein we present the effect of artificially imposed topological constraint on calmodulin (CaM) backbone dynamics and its molecular recognition behavior. While backbone dynamics of CaM remain largely unperturbed, the thermodynamic profile of CaM binding to the smooth-muscle myosin light-chain kinase (smMLCK) peptide is modulated significantly.

Graphical abstract: Binding and backbone dynamics of protein under topological constraint: calmodulin as a model system

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Publication details

The article was received on 18 May 2018, accepted on 19 Jul 2018 and first published on 25 Jul 2018


Article type: Communication
DOI: 10.1039/C8CC03977A
Citation: Chem. Commun., 2018,54, 8917-8920
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    Binding and backbone dynamics of protein under topological constraint: calmodulin as a model system

    P. Katyal, Y. Yang, Y. Fu, J. Iandosca, O. Vinogradova and Y. Lin, Chem. Commun., 2018, 54, 8917
    DOI: 10.1039/C8CC03977A

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